The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.

@article{Smith2013TheEU,
  title={The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.},
  author={Matthew C Smith and Kenneth Matthew Scaglione and Victoria A. Assimon and Srikanth Patury and Andrea D. Thompson and Chad A Dickey and Daniel R Southworth and Henry L. Paulson and Jason E. Gestwicki and Erik R.P. Zuiderweg},
  journal={Biochemistry},
  year={2013},
  volume={52 32},
  pages={5354-64}
}
The E3 ubiquitin ligase CHIP (C-terminus of Hsc70 Interacting Protein, a 70 kDa homodimer) binds to the molecular chaperone Hsc70 (a 70 kDa monomer), and this complex is important in both the ubiquitination of Hsc70 and the turnover of Hsc70-bound clients. Here we used NMR spectroscopy, biolayer interferometry, and fluorescence polarization to characterize the Hsc70-CHIP interaction. We found that CHIP binds tightly to two molecules of Hsc70 forming a 210 kDa complex, with a Kd of approximately… CONTINUE READING

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